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1slq

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{{STRUCTURE_1slq| PDB=1slq | SCENE= }}
{{STRUCTURE_1slq| PDB=1slq | SCENE= }}
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'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT'''
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===Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT===
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==Overview==
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Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes. We have determined the crystal structure, at 3.2 A resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a approximately 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses.
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(as it appears on PubMed at http://www.pubmed.gov), where 15329727 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15329727}}
==About this Structure==
==About this Structure==
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[[Category: Non-enveloped virus]]
[[Category: Non-enveloped virus]]
[[Category: Spike protein]]
[[Category: Spike protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:51:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:22:45 2008''

Revision as of 04:22, 29 July 2008

Template:STRUCTURE 1slq

Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT

Template:ABSTRACT PUBMED 15329727

About this Structure

1SLQ is a Single protein structure of sequence from Rhesus rotavirus. Full crystallographic information is available from OCA.

Reference

Structural rearrangements in the membrane penetration protein of a non-enveloped virus., Dormitzer PR, Nason EB, Prasad BV, Harrison SC, Nature. 2004 Aug 26;430(7003):1053-8. PMID:15329727

Page seeded by OCA on Tue Jul 29 07:22:45 2008

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